9mr8

Structure of D421-Truncated Tau Fibril

Method: ELECTRON MICROSCOPY Dmax: 102.6 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Microtubule-associated protein tau

Homo sapiens

UniProt P10636

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain C; UniProt 590–679 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 590–679 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

248 other PDB entries and 269 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–90; UniProt 590–679

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9mr8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mr8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mr8
Deposition date deposition_date2025-01-07
Structure title titleStructure of D421-Truncated Tau Fibril
Keywords keywordsTau, amyloid fibrils, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier27.26
Radius of gyration Rg (electron density) rg_electron27.99
Forward intensity I(0) i01904460.00
Molecular weight molecular_weight9638.0 kDa
Excluded volume excluded_volume12084 ų
Envelope volume envelope_volume20251 ų
Hydration-shell volume shell_volume7833 ų
Envelope diameter envelope_diameter104.1
Shell Rg shell_rg27.21
Envelope Rg envelope_rg28.08
Shape Rg shape_rg28.08
Total Rg total_rg27.59
Total atoms total_atoms1386
Residues n_residues90
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax102.6
Rg (real space) rg_real27.97
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real1.9040e+06
I(0) uncertainty (real space) i0_real_error3.1360e+04
Rg (reciprocal space) rg_reciprocal27.75
I(0) (reciprocal space) i0_reciprocal1904000.0000
Solution quality estimate total_estimate0.7401
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.674
Kurtosis Kurtosis kurtosis-0.147
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha200500.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.493; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.198; Smooth: 0.938

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)